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Literature summary for 3.4.14.5 extracted from

  • Ogata, S.; Misumi, Y.; Ikehara, Y.
    Primary structure of rat liver dipeptidyl peptidase IV deduced from its cDNA and identification of the NH2-terminal signal sequence as the membrane-anchoring domain (1989), J. Biol. Chem., 264, 3596-3601.
    View publication on PubMed
Search for more literature for 3.4.14.5

Cloned(Commentary)

Cloned (Comment) Organism
-
 Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasmic membrane
-
 Rattus norvegicus
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
88107
-
 x * 88107, calculation from nucleotide sequence Rattus norvegicus
105000
-
 x * 105000, enzyme form sDPP, SDS-PAGE Rattus norvegicus
109000
-
 x * 109000, enzyme form mDPP, SDS-PAGE Rattus norvegicus
160000 180000 gel filtration Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
no modification the signal peptide of dipeptidyl peptidase IV is not cleaved off during biosynthesis but functions as the membrane-anchoring domain even in the mature form Rattus norvegicus
side-chain modification eight potential N-linked glycosylation sites Rattus norvegicus

Purification (Commentary)

Purification (Comment) Organism
two enzyme forms: a plasma membrane form, mDPP, and a soluble form, sDPP Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Subunits

Subunits Comment Organism
? x * 105000, enzyme form sDPP, SDS-PAGE Rattus norvegicus
? x * 109000, enzyme form mDPP, SDS-PAGE Rattus norvegicus
? x * 88107, calculation from nucleotide sequence Rattus norvegicus